ID C8XPB1_9FLAV Unreviewed; 3417 AA. AC C8XPB1; DT 03-NOV-2009, integrated into UniProtKB/TrEMBL. DT 03-NOV-2009, sequence version 1. DT 16-APR-2014, entry version 39. DE SubName: Full=Polyprotein; OS Zika virus. OC Viruses; ssRNA positive-strand viruses, no DNA stage; Flaviviridae; OC Flavivirus; Spondweni virus group. OX NCBI_TaxID=64320; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=MR 766; RA Brisbarre N., Moureau G., Grard G., de Lamballerie X.; RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=MR 766; RX PubMed=19741066; DOI=10.1099/vir.0.014506-0; RA Grard G., Moureau G., Charrel R.N., Holmes E.C., Gould E.A., RA de Lamballerie X.; RT "Genomics and evolution of Aedes-borne flaviviruses."; RL J. Gen. Virol. 91:87-94(2010). CC -!- FUNCTION: Envelope protein E binding to host cell surface receptor CC is followed by virus internalization through clathrin-mediated CC endocytosis. Envelope protein E is subsequently involved in CC membrane fusion between virion and host late endosomes. CC Synthesized as a homodimer with prM which acts as a chaperone for CC envelope protein E. After cleavage of prM, envelope protein E CC dissociate from small envelope protein M and homodimerizes (By CC similarity). CC -!- CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate CC + RNA(n+1). CC -!- SUBCELLULAR LOCATION: Virion membrane; Multi-pass membrane CC protein. Host endoplasmic reticulum membrane; Multi-pass membrane CC protein (By similarity). CC -!- SIMILARITY: Contains RdRp catalytic domain. CC -!- SIMILARITY: Contains helicase ATP-binding domain. CC -!- SIMILARITY: Contains helicase C-terminal domain. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; DQ859059; ABI54475.1; -; Genomic_RNA. DR ProteinModelPortal; C8XPB1; -. DR GO; GO:0044167; C:host cell endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0019028; C:viral capsid; IEA:UniProtKB-KW. DR GO; GO:0019031; C:viral envelope; IEA:UniProtKB-KW. DR GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0008026; F:ATP-dependent helicase activity; IEA:InterPro. DR GO; GO:0003725; F:double-stranded RNA binding; IEA:InterPro. DR GO; GO:0004482; F:mRNA (guanine-N7-)-methyltransferase activity; IEA:InterPro. DR GO; GO:0004483; F:mRNA (nucleoside-2'-O-)-methyltransferase activity; IEA:InterPro. DR GO; GO:0003724; F:RNA helicase activity; IEA:InterPro. DR GO; GO:0003968; F:RNA-directed RNA polymerase activity; IEA:UniProtKB-KW. DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro. DR GO; GO:0070008; F:serine-type exopeptidase activity; IEA:InterPro. DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro. DR GO; GO:0075512; P:clathrin-mediated endocytosis of virus by host cell; IEA:UniProtKB-KW. DR GO; GO:0039654; P:fusion of virus membrane with host endosome membrane; IEA:UniProtKB-KW. DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW. DR GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro. DR GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW. DR Gene3D; 2.60.40.350; -; 1. DR Gene3D; 2.60.98.10; -; 2. DR Gene3D; 3.30.387.10; -; 1. DR Gene3D; 3.40.50.300; -; 2. DR InterPro; IPR011492; DEAD_Flavivir. DR InterPro; IPR000069; Env_glycoprot_M_flavivir. DR InterPro; IPR013755; Flav_gly_cen_dom_subdom1. DR InterPro; IPR001122; Flavi_capsidC. DR InterPro; IPR026470; Flavi_E_Stem/Anchor_dom. DR InterPro; IPR001157; Flavi_NS1. DR InterPro; IPR000752; Flavi_NS2A. DR InterPro; IPR000487; Flavi_NS2B. DR InterPro; IPR000404; Flavi_NS4A. DR InterPro; IPR001528; Flavi_NS4B. DR InterPro; IPR002535; Flavi_propep. DR InterPro; IPR000336; Flavivir/Alphavir_Ig-like. DR InterPro; IPR001850; Flavivirus_NS3_S7. DR InterPro; IPR027287; Flavovir_Ig-like. DR InterPro; IPR014412; Gen_Poly_FLV. DR InterPro; IPR011998; Glycoprot_cen/dimer. DR InterPro; IPR013754; GlyE_dim. DR InterPro; IPR014001; Helicase_ATP-bd. DR InterPro; IPR001650; Helicase_C. DR InterPro; IPR014756; Ig_E-set. DR InterPro; IPR026490; mRNA_cap_0/1_MeTrfase. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR000208; RNA-dir_pol_flavivirus. DR InterPro; IPR007094; RNA-dir_pol_PSvirus. DR InterPro; IPR002877; rRNA_MeTrfase_FtsJ_dom. DR InterPro; IPR009003; Trypsin-like_Pept_dom. DR Pfam; PF01003; Flavi_capsid; 1. DR Pfam; PF07652; Flavi_DEAD; 1. DR Pfam; PF02832; Flavi_glycop_C; 1. DR Pfam; PF00869; Flavi_glycoprot; 1. DR Pfam; PF01004; Flavi_M; 1. DR Pfam; PF00948; Flavi_NS1; 1. DR Pfam; PF01005; Flavi_NS2A; 1. DR Pfam; PF01002; Flavi_NS2B; 1. DR Pfam; PF01350; Flavi_NS4A; 1. DR Pfam; PF01349; Flavi_NS4B; 1. DR Pfam; PF00972; Flavi_NS5; 1. DR Pfam; PF01570; Flavi_propep; 1. DR Pfam; PF01728; FtsJ; 1. DR Pfam; PF00271; Helicase_C; 1. DR Pfam; PF00949; Peptidase_S7; 1. DR PIRSF; PIRSF003817; Gen_Poly_FLV; 1. DR SMART; SM00487; DEXDc; 1. DR SMART; SM00490; HELICc; 1. DR SUPFAM; SSF50494; SSF50494; 1. DR SUPFAM; SSF52540; SSF52540; 2. DR SUPFAM; SSF56983; SSF56983; 1. DR SUPFAM; SSF81296; SSF81296; 1. DR TIGRFAMs; TIGR04240; flavi_E_stem; 1. DR PROSITE; PS51527; FLAVIVIRUS_NS2B; 1. DR PROSITE; PS51528; FLAVIVIRUS_NS3PRO; 1. DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1. DR PROSITE; PS51194; HELICASE_CTER; 1. DR PROSITE; PS50507; RDRP_SSRNA_POS; 1. DR PROSITE; PS51591; RNA_CAP01_NS5_MT; 1. PE 3: Inferred from homology; KW ATP-binding; Capsid protein; KW Clathrin-mediated endocytosis of virus by host; Disulfide bond; KW Fusion of virus membrane with host endosomal membrane; KW Fusion of virus membrane with host membrane; Helicase; KW Host endoplasmic reticulum; Host membrane; Host-virus interaction; KW Hydrolase; Membrane; Nucleotide-binding; Nucleotidyltransferase; KW Protease; RNA-directed RNA polymerase; Serine protease; Transferase; KW Transmembrane; Transmembrane helix; Viral attachment to host cell; KW Viral envelope protein; Viral penetration into host cytoplasm; KW Viral RNA replication; Virion; Virus endocytosis by host; KW Virus entry into host cell. SQ SEQUENCE 3417 AA; 378191 MW; 3B9B8F66DAA096F9 CRC64; MKNPKKKSGG FRIVNMLKRG VARVNPLGGL KRLPAGLLLG HGPIRMVLAI LAFLRFTAIK PSLGLINRWG TVGKKEAMEI IKKFKKDLAA MLRIINARKE RKRRGADTSI GIVGLLLTTA MAAEITRRGS AYYMYLDRSD AGKAISFATT LGVNKCHVQI MDLGHMCDAT MSYECPMLDE GVEPDDVDCW CNTTSTWVVY GTCHHKKGEA RRSRRAVTLP SHSTRKLQTR SQTWLESREY TKHLIKVENW IFRNPGFTLV AVAIAWLLGS STSQKVIYLV MILLIAPAYS IRCIGVSNRD FVEGMSGGTW VDVVLEHGGC VTVMAQDKPT VDIELVTTTV SNMAEVRSYC YEASISDMAS DSRCPTQGEA YLDKQSDTQY VCKRTLVDRG WGNGCGLFGK GSLVTCAKFT CSKKMTGKSI QPENLEYRIM LSVHGSQHSG MIVNDENRAK VEVTPNSPRA EATLGGFGSL GLDCEPRTGL DFSDLYYLTM NNKHWLVHKE WFHDIPLPWH AGADTGTPHW NNKEALVEFK DAHAKRQTVV VLGSQEGAVH TALAGALEAE MDGAKGRLFS GHLKCRLKMD KLRLKGVSYS LCTAAFTFTK VPAETLHGTV TVEVQYAGTD GPCKVPAQMA VDMQTLTPVG RLITANPVIT ESTENSKMML ELDPPFGDSY IVIGVGDKKI THHWHRSGST IGKAFEATVR GAKRMAVLGD TAWDFGSVGG VFNSLGKGIH QIFGAAFKSL FGGMSWFSQI LIGTLLVWLG LNTKNGSISL TCLALGGVMI FLSTAVSADV GCSVDFSKKE TRCGTGVFVY NDVEAWRDRY KYHPDSPRRL AAAVKQAWEE GICGISSVSR MENIMWKSVE GELNAILEEN GVQLTVVVGS VKNPMWRGPQ RLPVPVNELP HGWKAWGKSY FVRAAKTNNS FVVDGDTLKE CPLKHRAWNS FLVEDHGFGV FHTSVWLKVR EDYSLECDPA VIGTAVKGKE AAHSDLGYWI ESEKNDTWRL KRAHLIEMKT CEWPKSHTLW TDGVEESDLI IPKSLAGPLS HHNTREGYRT QVKGPWHSEE LEIRFEECPG TKVHVEETCG TRGPSLRSTT ASGRVIEEWC CRECTMPPLS FRAKDGCWYG MEIRPRKEPE SNLVRSMVTA GSTDHMDHFS LGVLVILLMV QEGLKKRMTT KIIMSTSMAV LVAMILGGFS MSDLAKLVIL MGATFAEMNT GGDVAHLALV AAFKVRPALL VSFIFRANWT PRESMLLALA SCLLQTAISA LEGDLMVLVN GFALAWLAIR AMAVPRTDNI ALAILAALTP LARGTLLVAW RAGLATCGGF MLLSLKGKGS VKKNLPFVAA LGLTAVRIVD PINVVGLLLL TRSGKRSWPP SEVLTAVGLI CALAGGFAKA DIEMAGPMAA VGLLIVSYVV SGKSVDMYIE RAGDITWEKD AEVTGNSPRL DVALDESGDF SLVEEDGPPM REIILKVVLM AICGMNPIAI PFAAGAWYVY VKTGKRSGAL WDVPAPKEVK KGETTDGVYR VMTRRLLGST QVGVGVMQEG VFHTMWHVTK GAALRSGEGR LDPYWGDVKQ DLVSYCGPWK LDAAWDGVSE VQLLAVPPGE RARNIQTLPG IFKTKDGDIG AVALDYPAGT SGSPILDKCG RVIGLYGNGV VIKNGSYVSA ITQGKREEET PVECFEPSML KKKQLTVLDL HPGAGKTRRV LPEIVREAIK KRLRTVILAP TRVVAAEMEE ALRGLPVRYM TTAVKVTHSG TEIVDLMCHA TFTSRLLQPI RVPNYNLYIM DEAHFTDPSS IAARGYISTR VEMGEAAAIF MTATPPGTRD AFPDSNSPIM DTEVEVPERA WSSGFDWVTD HSGKTVWFVP SVRNGNEIAA CLTKAGKRVI QLSRKTFETE FQKTKNQEWD FVITTDISEM GANFKADRVI DSRRCLKPVI LDGERVILAG PMPVTHASAA QRRGRIGRNP NKPGDEYMYG GGCAETDEDH AHWLEARMLL DNIYLQDGLI ASLYRPEADK VAAIEGEFKL RTEQRKTFVE LMKRGDLPVW LAYQVASAGI TYTDRRWCFD GTTNNTIMED SVPAEVWTKY GEKRVLKPRW MDARVCSDHA ALKSFKEFAA GKRGAALGVM EALGTLPGHM TERFQEAIDN LAVLMRAETG SRPYKAAAAQ LPETLETIML LGLLGTVSLG IFFVLMRNKG IGKMGFEMVT LGASAWLMWL SEIEPARIAC VLIVVFLLLV VLIPEPEKQR SPQDNQMAII IMVAVGLLGL ITANELGWLE RTKNDIAHLM GKREEGTTVG FSMDIDLRPA SAWAIYAALT TLITPAVQHA VTTSYNNYSL MAMATQAGVL FGMGKGMPFY AWDLGVPLLM MGCYSQLTPL TLIVAIILLV AHYMYLIPGL QAAAARAAQK RTAAGIMKNP VVDGIVVTDI DTMTIDPQVE KKMGQVLLIA VAVSSAVLLR TAWGWGEAGA LITAATSTLW EGSPNKYWNS STATSLCNIF RGSYLAGASL IYTVTRNAGL VKRRGGGTGE TLGEKWKARL NQMSALEFYS YKKSGITEVC REEARRALKD GVATGGHAVS RGSAKLRWLV ERGYLQPYGK VVDLGCGRGG WSYYAATIRK VQEVRGYTKG GPGHEEPMLV QSYGWNIIRL KSGVDVFHMA AESCDTLLCD IGESSSSPEV EETRTLRVLS MVGDWLEKRP GAFCIKVLCP YTSTMMETME RLQRRYGGGL VRVPLSRNST HEMYWVSGAK SNIIKSVSTT SQLLLGRMDG PRRPVKYEED VNLGSGTRAV ASCAEAPNMK VIGRRIERIR SEHAETWFFD ENHPYRTWAY HGSYEAPTQG SASSLVNGVV RLLSKPWDVV TGVTGIAMTD TTPYGQQRVF KEKVDTRVPD PQEGTRQVMN MVASWLWKEL GKRKRPRVCT KEEFINKVRS NAALGAIFEE EKEWKTAVEA VNDPRFWALV DKEREHHLRG ECHSCVYNMM GKREKKQGEF GKAKGSRAIW YMWLGARFLE FEALGFLNED HWMGRENSGG GVEGLGLQRL GYVLEEMSRA PGGKMYADDT AGWDTRISKF DLENEALITN QMDEGHRTLA LAVIKYTYQN KVVKVLRPAE GGKTVMDIIS RQDQRGSGQV VTYALNTFTN LVVQLIRNME AEEVLEMQDL WLLRKPEKVT RWLQSSGWDR LKRMAVSGDD CVVKPIDDRF AHALRFLNDM GKVRKDTQEW KPSTGWSNWE EVPFCSHHFN KLHLKDGRSI VVPCRHQDEL IGRARVSPGA GWSIRETACL AKSYAQMWQL LYFHRRDLRL MANAICSAVP VDWVPTGRTT WSIHGKGEWM TTEDMLMVWN RVWIEENDHM EDKTPVTKWT DIPYLGKRED LWCGSLIGHR PRTTWAENIK DTVSMVRRII GDEEKYMDYL STQVRYLGEE GSTPGVL //